| IED ID | IndEnz0010001028 |
| Enzyme Type ID | esterase001028 |
| Protein Name |
Acyltransferase mokF EC 2.3.1.238 Lovastatin hydrolase Monacolin K biosynthesis protein F |
| Gene Name | mokF |
| Organism | Monascus pilosus (Red mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Monascus Monascus pilosus (Red mold) |
| Enzyme Sequence | MRQFLSSDRINSEIPQEKSEMVGFSDIDNSSRQIKEMEAAFRSAVKTGQIPGAVIMARDHSGRLNYTRCFGARTVVRDECNRLPPMQVDTPCRLASATKLLTTIMALQCVERGLVRLDETVDRLLPDLSAMKVLEGFDAAGEPKMRERKGKITLKHLLTHTSGLSYVFLHPLLREYMAKGHLQTAEKFGIQSRLAPPAVNDPGAEWIYGANLDWTGKLVERATGLDLEQYLQENICAPLNITDMTFKLQQRPDLLARRADQTHRNKADGRLRYDDSVYFRSDGDECFGGQGVFSGPESYMKVVHSLLQRDGRLLRPETVDLMFQPALDAQTEKQMNQHMDASPHINYGGPMPMVLRRSFGLGGMIALEDLDGQKWRRKGCLTFGGGPNIVWVMLLSALRFVFFFFFFFFFCSS |
| Enzyme Length | 413 |
| Uniprot Accession Number | Q3S2U2 |
| Absorption | |
| Active Site | ACT_SITE 96; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q9Y7D1 |
| Activity Regulation | |
| Binding Site | BINDING 93; /note=Monacolin J; /evidence=ECO:0000250|UniProtKB:Q9Y7D1; BINDING 193; /note=Monacolin J; /evidence=ECO:0000250|UniProtKB:Q9Y7D1; BINDING 208; /note=Monacolin J; /evidence=ECO:0000250|UniProtKB:Q9Y7D1; BINDING 278; /note=Monacolin J; /evidence=ECO:0000250|UniProtKB:Q9Y7D1; BINDING 386; /note=2-methylbutanoate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q9Y7D1 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + monacolin J carboxylate = holo-[2-methylbutanoate polyketide synthase] + lovastatin carboxylate; Xref=Rhea:RHEA:43064, Rhea:RHEA-COMP:10260, Rhea:RHEA-COMP:10261, ChEBI:CHEBI:64479, ChEBI:CHEBI:79035, ChEBI:CHEBI:79038, ChEBI:CHEBI:82764; EC=2.3.1.238; Evidence={ECO:0000250|UniProtKB:Q9Y7D1}; |
| DNA Binding | |
| EC Number | 2.3.1.238 |
| Enzyme Function | FUNCTION: Acyltransferase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535). Monakolin K biosynthesis is performed in two stages (PubMed:19693441). The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441). This PKS stage is completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441). Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity). Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441). Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441). {ECO:0000250|UniProtKB:Q0C8M2, ECO:0000303|PubMed:18578535, ECO:0000303|PubMed:19693441}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Polyketide biosynthesis; lovastatin biosynthesis. {ECO:0000250|UniProtKB:Q9Y7D1}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (5); Chain (1) |
| Keywords | Acyltransferase;Hydrolase;Transferase |
| Interact With | |
| Induction | INDUCTION: Expression is controlled by the monacolin K cluster transcription regulator mokH (PubMed:19968298). {ECO:0000269|PubMed:19968298}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:43064 |
| Cross Reference Brenda |